Mutation at the acidic residue-rich domain of eukaryotic initiation factor 2 (eIF2α)-associated glycoprotein p67 increases the protection of eIF2α phosphorylation during heat shock

Archives of Biochemistry and Biophysics

Volumn 413, Issue 1, 2003, Pages 116-122

  Datta, Bansidhar ^a   Datta, Rekha ^a  

^a KENT STATE UNIVERSITY   (United States)

Author keywords

eIF2 associated glycoprotein; eIF2 phosphorylation; Heat shock; Mutagenesis; p67; Protein synthesis initiation

Indexed keywords

ALANINE; AMINO ACID; ENZYME; EUKARYOTIC INITIATION FACTOR 2 ASSOCIATED GLYCOPROTEIN P67; GLYCOPROTEIN; INITIATION FACTOR 2; LYSINE; MUTANT PROTEIN; PHOSPHOPROTEIN; POLYCLONAL ANTIBODY; UNCLASSIFIED DRUG;

ACIDITY; AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; CORRELATION ANALYSIS; HEAT SHOCK; HEPATOMA CELL; MOLECULAR WEIGHT; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DETERMINATION; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN PHOSPHORYLATION; PROTEIN SYNTHESIS; PROTEIN SYNTHESIS INHIBITION; QUANTITATIVE ANALYSIS; RAT; REGULATORY MECHANISM; TUMOR CELL LINE;

EUKARYOTA;

EID: 0037404158     PISSN: 00039861     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0003-9861(03)00092-4     Document Type: Article

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